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Database: UniProt
Entry: K7ABU9_PANTR
LinkDB: K7ABU9_PANTR
Original site: K7ABU9_PANTR 
ID   K7ABU9_PANTR            Unreviewed;       583 AA.
AC   K7ABU9; A0A2J8M2C3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Complement factor I {ECO:0000313|EMBL:JAA15366.1, ECO:0000313|Ensembl:ENSPTRP00000075533.1};
GN   Name=CFI {ECO:0000313|EMBL:JAA15366.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000075533.1, ECO:0000313|VGNC:VGNC:579};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA15366.1};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000075533.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:JAA15366.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA02044.1}, and Smooth
RC   vascular {ECO:0000313|EMBL:JAA15366.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000075533.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR   EMBL; AACZ04021153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04021154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04021155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GABC01009294; JAA02044.1; -; mRNA.
DR   EMBL; GABF01006779; JAA15366.1; -; mRNA.
DR   RefSeq; XP_016807511.1; XM_016952022.1.
DR   RefSeq; XP_526653.2; XM_526653.5.
DR   MEROPS; S01.199; -.
DR   Ensembl; ENSPTRT00000077764.1; ENSPTRP00000075533.1; ENSPTRG00000031127.5.
DR   GeneID; 471271; -.
DR   CTD; 3426; -.
DR   VGNC; VGNC:579; CFI.
DR   GeneTree; ENSGT00930000151042; -.
DR   OrthoDB; 4629979at2759; -.
DR   Proteomes; UP000002277; Chromosome 4.
DR   Bgee; ENSPTRG00000031127; Expressed in liver and 20 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR048722; CFAI_FIMAC_N.
DR   InterPro; IPR048719; CFAI_KAZAL.
DR   InterPro; IPR003884; FacI_MAC.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24264:SF40; HYALURONAN-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   Pfam; PF21286; CFAI_FIMAC_N; 1.
DR   Pfam; PF21287; CFAI_KAZAL; 1.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   Pfam; PF00530; SRCR; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00057; FIMAC; 1.
DR   SMART; SM00192; LDLa; 2.
DR   SMART; SM00202; SR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 2.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 2.
DR   PROSITE; PS50287; SRCR_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..583
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015095785"
FT   DOMAIN          60..108
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          114..215
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          340..574
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        186..196
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        229..247
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        241..256
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        259..271
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        266..284
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        278..293
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   583 AA;  65892 MW;  1DEF06DABFBFC71F CRC64;
     MKLLHVFLLF LCFHLRFCKV TYTSQEDLVE KKCLAKKYTH LSCDKVFCQP WQRCIEGTCI
     CKLPYQCPKN GTAVCATNRR SFPTYCQQKS LECLRPGTKF LNNGTCTAEG KFSVSLKHGI
     TDSEGIVEVK LVDQDKTMFI CKSSWSMREA NVACLDLGFQ QGADTQRRFK LSDLSINSTE
     CLHVHCRGLE TSLAECTFTK RRTMGYQDLA DVVCYTQKAD SPMNDFFQCV NGKYISQMKA
     CDGINDCGDQ SDELCCKACQ GKSFHCKSGV CIPSQYQCNG EVDCITGEDE VGCEGFASVA
     QEETEILTAD MDAERRRIKS LLPKLSCGVK NRMHIRRKRI VGGKRAQLGD LPWQVAIKDA
     SGITCGGIYI GGCWILTAAH CLRASKTHRY QIWTRVVDWI HPDRKRIVIE HVDRIIFHEN
     YNAGTYQNDI ALIEMKKDGN KKDCELPRSI PACIPWSPYL FQPNDTCIVS GWGREKDNER
     VFSLQWGEVK LISNCSKFYG NRFYEKEMEC AGTYDGSIDA CKGDSGGPLV CMDANNVTYV
     WGVVSWGENC GKPEFPGVYT KVANYFDWIS YHVGRPFISQ YNV
//
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